Mutations within the cholecystokinin-B/gastrin receptor ligand 'pocket' interconvert the functions of nonpeptide agonists and antagonists.

doi:10.1124/mol.54.5.857

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Article

Mutations within the cholecystokinin-B/gastrin receptor ligand 'pocket' interconvert the functions of nonpeptide agonists and antagonists.

Molecular pharmacology - 1 Nov 1998

Bläker M, Ren Y, Gordon M C, Hsu J E, Beinborn M, Kopin A S

Abstract excerpt

We have reported previously that the transmembrane domains of the cholecystokinin-B/gastrin receptor (CCK-BR) comprise a putative ligand binding pocket. In the present study, we examined whether amino acid substitutions within the CCK-BR pocket altered the affinities and/or functional activities...

Topics

Animals
Benzodiazepines
Benzodiazepinones
Binding Sites
COS Cells
Cell Membrane
DNA, Complementary
Hormone Antagonists
Humans
Inositol Phosphates
Iodine Radioisotopes
Ligands
Mutagenesis, Site-Directed
Mutation
Phenylurea Compounds
Receptor, Cholecystokinin B
Receptors, Cholecystokinin
Sincalide

Source

Open in PubMed

Identifiers

PMID: 9804620
DOI: 10.1124/mol.54.5.857

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9804620-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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